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Islet amyloidea polypeptidis (IAPP, quae etiam amylin nota est) est formatio amyloidea isletae in specie 2 diabete, et toxicitas IAPP-inducta creditur ad iacturam massae β-cellulae consociatae cum proximis stadiis 2 diabete typorum.Formatio amyloidea islet etiam munus insita post translationem defectum habere potest.IAPP ut prohormona, polypeptide amyloidea pro-isleta (proIAPP), in granulis secretoriorum pancreaticorum aba-cellarum processit.Partim discursum formae proIAPP in depositis amyloideae inveniuntur;notabilis est medium 48-residuum, proIAPP(1-48), quod includit N-terminalem pro-extensionem, sed proprie processit ad C-terminum.Processus imperfectus munus habere potest in formatione islet amyloideae, promovendo interactiones cum proteoglycis sulfated matricis extracellulares, quae vicissim formationem amyloideam promovent.Ostendimus acidum fuchsin (3-(1-(4-amino-3-methyl-5-sulphonatophenyl) -1-(4-amino-3-sulphonatophenyl)methylenum) acidum cyclohexa-i,4-dienesulphonicum, simplex. triphenylum methyl derivativum sulfonatum, potens inhibitor formationis amyloideae per proIAPP(1-48) intermedia.Triphenyl methanum velocius derivativum magis complicatum viridis FCF {ethyl-[4-[[4-[ethyl-[(3-sulfophenyl) methyl]amino]phenyl]-(4-hydroxy-2-sulfophenyl)methylidene]-1-cyclohexa -2,5-dienylidene]-[(3-sulfophenyl)methyl]azani} formationem amyloideam ab IAPP vetat et intermedium proIAPP processus.Utraque composita formationem amyloideam inhibent mixtis intermedii proIAPP et exemplar glycosaminoglycani heparani sulfati.Acidum fuchsin etiam formationem glycosaminoglycan-mediatam amyloideae per maturam IAPP vetat.Facultas formationis amyloideae inhibendi non est simpliciter ex mixtis sulfonatis, quia sulfonatus inhibitor amyloidei, tramiprosatus non est inhibitor formationis amyloideae per proIAPP (1-48).